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α-Helix Unwinding as Force Buffer in Spectrins

Abstract : Spectrins are cytoskeletal proteins located at the inner face of the plasma membrane, making connections between membrane anchors and the actin cortex, and between actin filaments. Spectrins share a common structure forming a bundle of 3 a-helices and play a major role during cell deformation. Here, we used high-speed force spectroscopy and steered molecular dynamics simulations to understand the mechanical stability of spectrin revealing a molecular force buffering function. We find that spectrin acts as a soft spring at short extensions (70-100Å). Under continuous external stretching, its α-helices unwind leading to a viscous mechanical response over larger extensions (100-300Å), represented by a constant-force plateau in force/extension curves. This viscous force buffering emerges from a quasi-equilibrium competition between disruption and reformation of a-helical hydrogen bonds. Our results suggest
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Contributor : Felix Rico Connect in order to contact the contributor
Submitted on : Monday, April 22, 2019 - 10:34:23 PM
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Hirohide Takahashi, Felix Rico, Christophe Chipot, Simon Scheuring. α-Helix Unwinding as Force Buffer in Spectrins. ACS Nano, 2018, 12 (3), pp.2719-2727. ⟨10.1021/acsnano.7b08973⟩. ⟨hal-02106340⟩



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